ROX_STRVP
ID ROX_STRVP Reviewed; 476 AA.
AC F2R776;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Rifampicin monooxygenase {ECO:0000303|PubMed:29398560};
DE Short=RIFMO;
GN Name=rox {ECO:0000303|PubMed:29398560}; OrderedLocusNames=SVEN_0481;
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=953739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD
RC 04745;
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Chandra G., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.32 ANGSTROMS) IN COMPLEX WITH FAD AND RIFAMPICIN.
RX PubMed=29398560; DOI=10.1016/j.chembiol.2018.01.009;
RA Koteva K., Cox G., Kelso J.K., Surette M.D., Zubyk H.L., Ejim L.,
RA Stogios P., Savchenko A., Sorensen D., Wright G.D.;
RT "Rox, a Rifamycin Resistance Enzyme with an Unprecedented Mechanism of
RT Action.";
RL Cell Chem. Biol. 0:0-0(2018).
CC -!- FUNCTION: Monooxygenase that can modify rifampicin, thereby
CC inactivating its antibiotic activity. It constitutes a secondary
CC rifampicin resistance factor. {ECO:0000269|PubMed:29398560}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + O2 + rifamycin SV = H2O + NADP(+) + rifamycin SV para-
CC naphthoquinone carboxamide; Xref=Rhea:RHEA:58676, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:84571, ChEBI:CHEBI:142728;
CC Evidence={ECO:0000269|PubMed:29398560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58677;
CC Evidence={ECO:0000303|PubMed:29398560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADH + O2 + rifamycin SV = H2O + NAD(+) + rifamycin SV para-
CC naphthoquinone carboxamide; Xref=Rhea:RHEA:58688, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:84571, ChEBI:CHEBI:142728;
CC Evidence={ECO:0000269|PubMed:29398560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58689;
CC Evidence={ECO:0000303|PubMed:29398560};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:29398560};
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DR EMBL; FR845719; CCA53768.1; -; Genomic_DNA.
DR RefSeq; WP_015031687.1; NZ_CP029197.1.
DR PDB; 5VQB; X-ray; 3.39 A; A/B/C=1-476.
DR PDB; 6BRD; X-ray; 3.32 A; A/B/C=1-476.
DR PDBsum; 5VQB; -.
DR PDBsum; 6BRD; -.
DR AlphaFoldDB; F2R776; -.
DR SMR; F2R776; -.
DR EnsemblBacteria; CCA53768; CCA53768; SVEN_0481.
DR KEGG; sve:SVEN_0481; -.
DR PATRIC; fig|953739.5.peg.6049; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_20_1_11; -.
DR OMA; DTAHPYG; -.
DR Proteomes; UP000006854; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..476
FT /note="Rifampicin monooxygenase"
FT /id="PRO_0000446369"
FT BINDING 12
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305|PubMed:29398560,
FT ECO:0007744|PDB:5VQB, ECO:0007744|PDB:6BRD"
FT BINDING 31..32
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305|PubMed:29398560,
FT ECO:0007744|PDB:5VQB, ECO:0007744|PDB:6BRD"
FT BINDING 98
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305|PubMed:29398560,
FT ECO:0007744|PDB:5VQB, ECO:0007744|PDB:6BRD"
FT BINDING 156
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305|PubMed:29398560,
FT ECO:0007744|PDB:5VQB, ECO:0007744|PDB:6BRD"
FT BINDING 196
FT /ligand="rifampicin"
FT /ligand_id="ChEBI:CHEBI:71365"
FT /evidence="ECO:0000305|PubMed:29398560,
FT ECO:0007744|PDB:5VQB, ECO:0007744|PDB:6BRD"
FT BINDING 213
FT /ligand="rifampicin"
FT /ligand_id="ChEBI:CHEBI:71365"
FT /evidence="ECO:0000305|PubMed:29398560,
FT ECO:0007744|PDB:5VQB, ECO:0007744|PDB:6BRD"
FT BINDING 277
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305|PubMed:29398560,
FT ECO:0007744|PDB:5VQB, ECO:0007744|PDB:6BRD"
FT BINDING 290..291
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000305|PubMed:29398560,
FT ECO:0007744|PDB:5VQB, ECO:0007744|PDB:6BRD"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6BRD"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:6BRD"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:5VQB"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:6BRD"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:6BRD"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:6BRD"
FT HELIX 98..111
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:6BRD"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:6BRD"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:5VQB"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:6BRD"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 208..217
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:6BRD"
FT HELIX 231..242
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:6BRD"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:6BRD"
FT HELIX 289..308
FT /evidence="ECO:0007829|PDB:6BRD"
FT TURN 314..317
FT /evidence="ECO:0007829|PDB:6BRD"
FT HELIX 318..340
FT /evidence="ECO:0007829|PDB:6BRD"
FT HELIX 346..358
FT /evidence="ECO:0007829|PDB:6BRD"
FT HELIX 362..372
FT /evidence="ECO:0007829|PDB:6BRD"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:5VQB"
FT TURN 386..389
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:6BRD"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:5VQB"
FT STRAND 411..418
FT /evidence="ECO:0007829|PDB:6BRD"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 429..433
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:6BRD"
FT STRAND 450..457
FT /evidence="ECO:0007829|PDB:6BRD"
FT HELIX 459..470
FT /evidence="ECO:0007829|PDB:6BRD"
SQ SEQUENCE 476 AA; 52402 MW; CD6F152CAF886800 CRC64;
MFDVIVVGGG PTGLMLAGEL RLHGVRVLVL EKETEPTRQS RAQGLHVRSI EVMAQRGLLE
RFLERGHTVA VGGFFAGLAT SWPERLDTAH SYVLAVPQVI TEQLLAEHAT ALGAEIRRGR
ALVGLRQDED GVTVDLADGE QLRARYVVGC DGGRSTVRKL LGVAFPGEPS RVETLLGEME
MTASQEELTS VMTEVRKTQQ RFGAMPLGDG VFRVVVPAEG VAEDRTASPT LDEFKQQLRA
HAGTDFGVHS PRWLSRFGDA TRQAERYRVD RVFLAGDAAH IHPPTGGQGL NLGIQDAFNL
GWKLAAEVDG WAPEGLLDTY HAERHPVATE VLDNTRAQIQ LMSTEPGPQA VRRLMAELVE
FENVNRYLIE KITAISVRYD VGEGHELLGR RMRDLALKHG RLYERMHEGR GLLLDQTGRL
SVAGWEDRVD HVVEVSEELD VPAVLLRPDG HVVWAGEDQQ ELLTRMPAWF GAATAG
